hemoglobin

the oxygen-carrying pigment of red blood cells that gives them their red color and serves to convey oxygen to the tissues: occurs in reduced form (deoxyhemoglobin) in venous blood and in combination with oxygen (oxyhemoglobin) in arterial blood. Symbol: Hb Cf. heme.

[1865-70; earlier hematoglobulin. See HEMO-, GLOBULIN]

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Protein in the blood of many animals (in vertebrates it is in red blood cells) that transports oxygen from the lungs to the tissues.

It is bright red when combined with oxygen and purple-blue in the deoxygenated state. Each molecule is made up of a globin (a type of protein) and four heme groups. Heme, a complex heterocyclic compound, is an organic molecule derived from porphyrin with an iron atom at the centre. Variant hemoglobins (see sickle-cell anemia; hemoglobinopathy) can be used to trace past human migrations and to study genetic relationships among populations.

iron-containing protein in the blood of many animals—in the red blood cells (erythrocytes (erythrocyte)) of vertebrates—that transports oxygen to the tissues.
Hemoglobin forms an unstable, reversible bond with oxygen; in the oxygenated state it is called oxyhemoglobin and is bright red; in the reduced state it is purplish blue.

Hemoglobin develops in cells in the bone marrow that become red blood cells. When red cells die, hemoglobin is broken up: iron is salvaged, transported to the bone marrow by proteins called transferrins (transferrin), and used again in the production of new red blood cells; the remainder of the hemoglobin forms the basis of bilirubin, a chemical that is excreted into the bile and gives the feces their characteristic yellow-brown colour.

Each hemoglobin molecule is made up of four heme groups surrounding a globin group, forming a tetrahedral structure. Heme, which accounts for only 4 percent of the weight of the molecule, is composed of a ringlike organic compound known as a porphyrin to which an iron atom is attached. It is the iron atom that binds oxygen as the blood travels between the lungs and the tissues. There are four iron atoms in each molecule of hemoglobin, which accordingly can bind four atoms of oxygen. Globin consists of two linked pairs of polypeptide chains.

Hemoglobin S is a variant form of hemoglobin that is present in persons who have sickle cell anemia, a severe, hereditary form of anemia in which the cells become crescent-shaped when oxygen is lacking. The sickling trait is found almost exclusively in people of African descent.

hemoglobin C — n an abnormal hemoglobin that differs from hemoglobin A in having a lysine residue substituted for the glutamic acid residue at position 6 in two of the four polypeptide chains making up the hemoglobin molecule * * * a common abnormal hemoglobin… … Medical dictionary

Hemoglobin C — (abbreviated as Hb C or HbC ) is an abnormal hemoglobin with substitution of a lysine residue for glutamic acid residue at the 6th position of the β globin chain. [ [http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 a=141900… … Wikipedia

Hemoglobin A2 — is a normal variant of hemoglobin A that consists of two alpha and two delta chains and is found in small quantity in normal human blood. Hemoglobin A2 may be increased in beta thalassemia.External links* … Wikipedia

hemoglobin A — n the hemoglobin in the red blood cells of the normal human adult that consists of two alpha chains and two beta chains * * * normal adult hemoglobin, composed of two α and two β chains, α2Aβ2A … Medical dictionary

Hemoglobin — Hem o*glo bin, n. [Hemo + globe.] (Physiol.) The normal coloring matter of the red blood corpuscles of vertebrate animals. It is composed of hematin and globulin, and is also called {h[ae]matoglobulin}. In arterial blood, it is always combined… … The Collaborative International Dictionary of English